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P28298 (ACEA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate lyase

Short name=ICL
Short name=Isocitrase
Short name=Isocitratase
EC=4.1.3.1
Gene names
Name:acuD
ORF Names:AN5634
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Isocitrate = succinate + glyoxylate.

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2.

Subunit structure

Homotetramer.

Subcellular location

Glyoxysome.

Induction

By acetate.

Sequence similarities

Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538Isocitrate lyase
PRO_0000068790

Sites

Active site2061

Experimental info

Sequence conflict171Missing in CAA44572. Ref.1
Sequence conflict681Missing in CAA44572. Ref.1
Sequence conflict1571A → T in CAA44572. Ref.1

Secondary structure

.................................................................................... 538
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28298 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 21B5B56E5345681E

FASTA53860,321
        10         20         30         40         50         60 
MSYIEEEDQR YWDEVAAVKN WWKDSRWRYT KRPFTAEQIV AKRGNLKIEY PSNVQAKKLW 

        70         80         90        100        110        120 
GILERNFKNK EASFTYGCLD PTMVTQMAKY LDTVYVSGWQ SSSTASSTDE PSPDLADYPM 

       130        140        150        160        170        180 
NTVPNKVNHL WMAQLFHDRK QREERMTTPK DQRHKVANVD YLRPIIADAD TGHGGLTAVM 

       190        200        210        220        230        240 
KLTKLFVERG AAGIHIEDQA PGTKKCGHMA GKVLVPISEH INRLVAIRAQ ADIMGTDLLA 

       250        260        270        280        290        300 
IARTDSEAAT LITSTIDHRD HPFIIGSTNP DIQPLNDLMV MAEQAGKNGA ELQAIEDEWL 

       310        320        330        340        350        360 
AKAGLKLFND AVVDAINNSP LPNKKAAIEK YLTQSKGKSN LEARAIAKEI AGTDIYFDWE 

       370        380        390        400        410        420 
APRTREGYYR YQGGTQCAIN RAVAYAPFAD LIWMESKLPD YKQAKEFADG VHAVWPEQKL 

       430        440        450        460        470        480 
AYNLSPSFNW KKAMPRDEQE TYIKRLGALG YAWQFITLAG LHTTALISDT FAKAYAKQGM 

       490        500        510        520        530 
RAYGELVQEP EMANGVDVVT HQKWSGANYV DNMLKMITGG VSSTAAMGKG VTEDQFKS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the glyoxysomal isocitrate lyase genes of Aspergillus nidulans (acuD) and Neurospora crassa (acu-3)."
Gainey L.D.S., Connerton I.F., Lewis E.H., Turner G., Ballance D.J.
Curr. Genet. 21:43-47(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: R153.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans."
Britton K.L., Langridge S.J., Baker P.J., Weeradechapon K., Sedelnikova S.E., De Lucas J.R., Rice D.W., Turner G.
Structure 8:349-362(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62696 Genomic DNA. Translation: CAA44572.1.
AACD01000098 Genomic DNA. Translation: EAA62727.1.
BN001305 Genomic DNA. Translation: CBF81510.1.
PIRS26857.
RefSeqXP_663238.1. XM_658146.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQUX-ray2.80A1-538[»]
ProteinModelPortalP28298.
SMRP28298. Positions 2-520.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00003436.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003436; CADANIAP00003436; CADANIAG00003436.
GeneID2871925.
KEGGani:AN5634.2.

Phylogenomic databases

eggNOGCOG2224.
HOGENOMHOG000238475.
KOK01637.
OMAALISHQF.
OrthoDBEOG73Z331.

Enzyme and pathway databases

UniPathwayUPA00703; UER00719.

Family and domain databases

Gene3D3.20.20.60. 2 hits.
InterProIPR006254. Isocitrate_lyase.
IPR018523. Isocitrate_lyase_ph_CS.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERPTHR21631:SF3. PTHR21631:SF3. 1 hit.
PfamPF00463. ICL. 1 hit.
[Graphical view]
PIRSFPIRSF001362. Isocit_lyase. 1 hit.
SUPFAMSSF51621. SSF51621. 1 hit.
TIGRFAMsTIGR01346. isocit_lyase. 1 hit.
PROSITEPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP28298.

Entry information

Entry nameACEA_EMENI
AccessionPrimary (citable) accession number: P28298
Secondary accession number(s): C8VFW4, Q5B1E6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 1, 2007
Last modified: May 14, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways